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Journal of Bacteriology, November 2006, p. 7521-7530, Vol. 188, No. 21
0021-9193/06/$08.00+0 doi:10.1128/JB.00943-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
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University of Florida, Department of Microbiology and Cell Science, Gainesville, Florida 32611-0700,1 University of Florida, Proteomics Core Facility, ICBR, Gainesville, Florida 32610-01562
Received 29 June 2006/ Accepted 20 August 2006
20S proteasomes are large, multicatalytic proteases that play an important role in intracellular protein degradation. The barrel-like architecture of 20S proteasomes, formed by the stacking of four heptameric protein rings, is highly conserved from archaea to eukaryotes. The outer two rings are composed of
-type subunits, and the inner two rings are composed of ß-type subunits. The halophilic archaeon Haloferax volcanii synthesizes two different
-type proteins,
1 and
2, and one ß-type protein that assemble into at least two 20S proteasome subtypes. In this study, we demonstrate that all three of these 20S proteasomal proteins (
1,
2, and ß) are modified either post- or cotranslationally. Using electrospray ionization quadrupole time-of-flight mass spectrometry, a phosphorylation site of the ß subunit was identified at Ser129 of the deduced protein sequence. In addition,
1 and
2 contained N-terminal acetyl groups. These findings represent the first evidence of acetylation and phosphorylation of archaeal proteasomes and are one of the limited examples of post- and/or cotranslational modification of proteins in this unusual group of organisms.
Published ahead of print on 1 September 2006.
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